ID   A0A6L8PY92_BACAN        Unreviewed;       152 AA.
AC   A0A6L8PY92; A0A2P0HJR8; E9R926; E9R927; Q6HSJ8; Q6KLU3; Q81L44;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Iron Transport-associated domain protein {ECO:0000313|EMBL:AAT33910.1};
GN   OrderedLocusNames=GBAA_4788 {ECO:0000313|EMBL:AAT33910.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT33910.1, ECO:0000313|Proteomes:UP000000594};
RN   [1] {ECO:0000313|EMBL:AAT33910.1, ECO:0000313|Proteomes:UP000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [2] {ECO:0007829|PDB:3SIK, ECO:0007829|PDB:3SZ6}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-146 IN COMPLEX WITH HEME B.
RX   PubMed=22412371; DOI=10.1371/journal.ppat.1002559;
RA   Ekworomadu M.T., Poor C.B., Owens C.P., Balderas M.A., Fabian M.,
RA   Olson J.S., Murphy F., Bakkalbasi E., Honsa E.S., He C., Goulding C.W.,
RA   Maresso A.W.;
RT   "Differential function of lip residues in the mechanism and biology of an
RT   anthrax hemophore.";
RL   PLoS Pathog. 8:e1002559-e1002559(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor
CC       {ECO:0000256|ARBA:ARBA00004168}.
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DR   EMBL; AE017334; AAT33910.1; -; Genomic_DNA.
DR   RefSeq; WP_000476161.1; NZ_WXXJ01000026.1.
DR   PDB; 3SIK; X-ray; 2.15 A; A/B=27-152.
DR   PDB; 3SZ6; X-ray; 1.80 A; A/B=26-146.
DR   AlphaFoldDB; A0A6L8PY92; -.
DR   SMR; A0A6L8PY92; -.
DR   GeneID; 45024419; -.
DR   KEGG; banh:HYU01_23335; -.
DR   KEGG; bar:GBAA_4788; -.
DR   PATRIC; fig|1392.230.peg.4718; -.
DR   OMA; MVMNRFE; -.
DR   OrthoDB; 2413751at2; -.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06920; NEAT; 1.
DR   Gene3D; 2.60.40.1850; -; 1.
DR   InterPro; IPR006635; NEAT_dom.
DR   InterPro; IPR037250; NEAT_dom_sf.
DR   PANTHER; PTHR37824; IRON-REGULATED SURFACE DETERMINANT PROTEIN C; 1.
DR   PANTHER; PTHR37824:SF1; IRON-REGULATED SURFACE DETERMINANT PROTEIN C; 1.
DR   Pfam; PF05031; NEAT; 1.
DR   SMART; SM00725; NEAT; 1.
DR   SUPFAM; SSF158911; NEAT domain-like; 1.
DR   PROSITE; PS50978; NEAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3SIK, ECO:0007829|PDB:3SZ6};
KW   Heme {ECO:0007829|PDB:3SIK}; Iron {ECO:0007829|PDB:3SIK};
KW   Metal-binding {ECO:0007829|PDB:3SIK};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..152
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039102127"
FT   DOMAIN          33..152
FT                   /note="NEAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50978"
FT   BINDING         53
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0007829|PDB:3SIK"
FT   BINDING         54
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0007829|PDB:3SIK"
FT   BINDING         136
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:3SIK"
SQ   SEQUENCE   152 AA;  17234 MW;  5896DB4E53317C8C CRC64;
     MFKQFKMIIA VFAVLFTFIA TLGLQDAKAA TKLADGKYNI AFTVWKGDKD ESSRMNRYFE
     SPATLTVKNG KQYVSFKVKD STSIKSFQVE KDGQFVETTV LSENKKDNTR VVEFEVADLS
     KKLNGKVKIN IPIINYNASY DIRFVFDGNS IK
//